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Two functionally distinct myosin heavy chain isoforms in slow skeletal muscle fibres
Author(s) -
Galler Stefan,
Hilber Karlheinz,
Gohlsch Bärbel,
Pette Dirk
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00556-5
Subject(s) - myosin , gene isoform , skeletal muscle , major histocompatibility complex , myh7 , biophysics , chemistry , microbiology and biotechnology , biology , biochemistry , anatomy , myosin light chain kinase , gene
The head part of the myosin heavy chain (MHC) represents the essential component of the molecular force‐generating system of muscle [1–3]. To date, three fast but only one slow MHC isoforms have been identified in adult mammalian limb muscles [4, 5]. We show here two functionally different slow MHC isoforms, MHCIβ and MHCIa, coexisting in a considerable fraction of slow fibres of rabbit plantaris muscle. The two isoforms exhibit distinct electrophoretic mobilities and different kinetic properties. Thus, as it is known for the fast muscle, also the slow muscle seems to use different MHC isoforms in order to fulfil different functional demands.